[Lys(Ac)12]-Histone H4 (1-20)

Product Name: [Lys(Ac)12]-Histone H4 (1-20)

Sequence One Letter Code: SGRGKGGKGLG-K(Ac)-GGAKRHRK

Sequence Three Letter Code: H-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys(Ac)-Gly-Gly-Ala-Lys-Arg-His-Arg-Lys-OH

Molecular Weight: 2034.5

Purity: 95%

Form: Lyophilized

Storage Conditions: - 20 °C

Research Area: epigenetics

Source / Species: human

Conjugation: Unconjugated

Code Nacres: NA.26

Application: This peptide corresponds to amino acids 1–20 of histone H4 and contains an acetyl modification at lysine 12 (H4K12ac), a histone mark associated with transcriptionally active chromatin and promoter regions. H4K12 acetylation has been linked to gene activation and the regulation of developmentally important genes, including transcripts retained in mature spermatozoa. By mimicking the native histone H4 N-terminal tail with a defined acetylation site, this peptide provides a useful substrate for studying histone acetyltransferase activity and acetyl-lysine recognition. It supports investigations of chromatin remodeling, epigenetic regulation, and promoter-associated histone modifications. The peptide is suitable for biochemical assays, antibody validation, and studies of chromatin structure and gene expression in developmental and reproductive biology.

Current Research: Histone modifications play a central role in the regulation of chromatin structure and gene expression. Among the various post-translational modifications that occur on histone proteins, lysine acetylation is one of the most extensively studied due to its strong association with transcriptionally active chromatin. The H4K12ac (1–20) peptide, representing the N-terminal region of histone H4 with an acetylated lysine at position 12, provides a valuable model substrate for investigating mechanisms of histone acetylation, chromatin remodeling, and epigenetic regulation. Histone H4 and the N-Terminal Tail Histones are the core protein components of nucleosomes, the structural units of chromatin that package DNA in eukaryotic cells. Each nucleosome consists of DNA wrapped around a histone octamer composed of two copies each of histones H2A, H2B, H3, and H4. The N-terminal tails of these histones extend outward from the nucleosome and are subject to numerous post-translational modifications, including acetylation, methylation, phosphorylation, and ubiquitination. These modifications influence chromatin organization by altering histone–DNA interactions or by recruiting chromatin-associated regulatory proteins. Because the histone H4 N-terminal tail contains several lysine residues that can be modified, it serves as an important regulatory platform in epigenetic signaling. The H4 (1–20) peptide corresponds to the first twenty amino acids of histone H4, a region that includes several lysine residues known to undergo regulatory modifications. In the H4K12ac variant, lysine 12 is specifically acetylated, reproducing a naturally occurring histone mark associated with active chromatin. Functional Significance of H4K12 Acetylation Acetylation of lysine residues on histones neutralizes the positive charge of the lysine side chain. This modification weakens the electrostatic interaction between histones and negatively charged DNA, resulting in a more relaxed chromatin structure that facilitates access for transcription factors and regulatory complexes. The H4K12ac modification has been widely linked to transcriptional activation and promoter-associated chromatin regions. Elevated levels of H4K12 acetylation are often observed near actively transcribed genes, where it contributes to a chromatin environment permissive for transcription. Beyond its role in transcriptional activation, H4K12 acetylation has also been implicated in developmental gene regulation. In particular, this modification has been associated with genes whose transcripts are retained in mature spermatozoa. These retained transcripts are thought to participate in early embryonic development, suggesting that histone modifications such as H4K12ac may play roles in epigenetic inheritance and reproductive biology. A Defined Substrate for Enzymatic Studies The H4K12ac (1–20) peptide is widely used as a biochemical substrate for studying histone acetyltransferases (HATs) and other enzymes that recognize or regulate acetylated lysine residues. Histone acetyltransferases catalyze the transfer of acetyl groups to lysine residues on histone tails, thereby modulating chromatin accessibility and transcriptional activity. Using a peptide that mimics the natural histone H4 tail with a defined acetylation site allows researchers to examine enzyme specificity, catalytic activity, and regulatory interactions in controlled biochemical assays. Such studies help clarify how acetylation patterns are established and maintained within chromatin. In addition, this peptide can serve as a substrate in experiments designed to evaluate histone deacetylase (HDAC) activity or to screen compounds that influence histone modification pathways. Studying Acetyl-Lysine Recognition Acetylated histone residues are recognized by specialized protein domains, including bromodomains, which bind acetyl-lysine motifs and recruit transcriptional regulators or chromatin remodeling complexes. The H4K12ac peptide provides a convenient system for investigating these recognition events. Biochemical and biophysical assays using the peptide can be used to characterize protein–histone interactions, determine binding affinities, and identify proteins that selectively recognize the H4K12ac modification. Understanding these interactions is essential for deciphering the complex networks that regulate chromatin structure and transcription. Applications in Chromatin and Epigenetics Research Because it mimics a native histone modification in a defined and simplified format, the H4K12ac (1–20) peptide is commonly used in a range of experimental applications. These include chromatin remodeling studies, enzyme activity assays, and investigations into the role of histone modifications in gene regulation. The peptide is also frequently employed for antibody validation and specificity testing, ensuring that antibodies targeting H4K12 acetylation selectively recognize the intended epigenetic mark. Reliable detection of histone modifications is essential for accurate analysis in chromatin immunoprecipitation and related assays. In addition, the peptide supports research focused on developmental biology and reproductive epigenetics, where histone modifications influence gene expression patterns during gametogenesis and early embryonic development. Supporting Advances in Epigenetic Research Defined histone peptides such as H4K12ac (1–20) provide researchers with precise tools for studying the molecular mechanisms that control chromatin dynamics and gene expression. By replicating the structure of the histone H4 N-terminal tail with a specific acetylation site, this peptide allows detailed investigation of epigenetic signaling pathways, chromatin-associated proteins, and transcriptional regulation mechanisms. As epigenetic research continues to expand, model substrates like the H4K12ac peptide remain essential for understanding how histone modifications shape chromatin function and influence biological processes ranging from development to disease.